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Exploring the envelope of life: Fold...

Luke, Kathryn A.

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Exploring the envelope of life: Folding and assembly reactions of hyper-thermostable co-chaperonin protein 10 from Aquifex aeolicus.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Exploring the envelope of life: Folding and assembly reactions of hyper-thermostable co-chaperonin protein 10 from Aquifex aeolicus./
作者:	Luke, Kathryn A.
面頁冊數:	107 p.
附註:	Adviser: Pernilla Wittung-Stafshede.
Contained By:	Dissertation Abstracts International68-03B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3256717

Exploring the envelope of life: Folding and assembly reactions of hyper-thermostable co-chaperonin protein 10 from Aquifex aeolicus.
Luke, Kathryn A.

Exploring the envelope of life: Folding and assembly reactions of hyper-thermostable co-chaperonin protein 10 from Aquifex aeolicus. - 107 p.

Adviser: Pernilla Wittung-Stafshede.

Thesis (Ph.D.)--Rice University, 2007.

The co-chaperonin protein 10 (cpn10) is a heptameric ring-shaped protein present in most organisms. It works in conjunction with the chaperonin protein 60 (cpn60) in an ATP-dependent process to assist folding a range of substrate polypeptides. Cpn10 from the hyper-thermophilic bacterium Aquifex aeolicus (Aacpn10) contains a 25-residue C-terminal extension in each monomer, not found in any other cpn10 protein. Both Aacpn10 and a mutant where the tail has been removed (Aacpn10del-25) adopt heptameric structures with similar thermal and chemical stabilities. In addition, the equilibrium and kinetic unfolding/dissociation and refolding/reassembly reactions are not affected by the presence or absence of the tail. The presence of the tail, however, increases the affinity between the subunits in the heptamer and limits the formation of ordered aggregates of the heptamers at high temperatures and high protein concentrations.Subjects--Topical Terms:

1019105
Biophysics, General.

Exploring the envelope of life: Folding and assembly reactions of hyper-thermostable co-chaperonin protein 10 from Aquifex aeolicus.
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245 1 0 $a Exploring the envelope of life: Folding and assembly reactions of hyper-thermostable co-chaperonin protein 10 from Aquifex aeolicus.
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500 $a Adviser: Pernilla Wittung-Stafshede.
500 $a Source: Dissertation Abstracts International, Volume: 68-03, Section: B, page: 1498.
502 $a Thesis (Ph.D.)--Rice University, 2007.
520 $a The co-chaperonin protein 10 (cpn10) is a heptameric ring-shaped protein present in most organisms. It works in conjunction with the chaperonin protein 60 (cpn60) in an ATP-dependent process to assist folding a range of substrate polypeptides. Cpn10 from the hyper-thermophilic bacterium Aquifex aeolicus (Aacpn10) contains a 25-residue C-terminal extension in each monomer, not found in any other cpn10 protein. Both Aacpn10 and a mutant where the tail has been removed (Aacpn10del-25) adopt heptameric structures with similar thermal and chemical stabilities. In addition, the equilibrium and kinetic unfolding/dissociation and refolding/reassembly reactions are not affected by the presence or absence of the tail. The presence of the tail, however, increases the affinity between the subunits in the heptamer and limits the formation of ordered aggregates of the heptamers at high temperatures and high protein concentrations.
520 $a Comparative studies on mesostable cpn10 heptamers from human mitochondria (hmcpn10) and Escherichia coli (GroES) reveal that the extreme stability of Aacpn10 originates from increased stability of individual monomers. The stability profile (i.e., the correlation between free energy and temperature) for Aacpn10 is shifted upwards (i.e., higher stability at each temperature) and to the right (i.e., maximum stability at higher temperature) as compared to that of GroES. This is the first thermodynamic analysis of how hyper-thermostability is achieved in an oligomeric protein system.
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